Cross-linking and lipid efflux properties of apoA-I mutants suggest direct association between apoA-I helices and ABCA1.
D064286:ATP Binding Cassette Transporter 1; D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019943:Amino Acid Substitution / Q000235:genetics; D000818:Animals; D016632:Apolipoprotein A-I / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D001667:Binding, Competitive / Q000235:genetics; D001692:Biological Transport / Q000235:genetics; D002460:Cell Line; D045744:Cell Line, Tumor; D008076:Cholesterol, HDL / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008956:Models, Chemical; D016296:Mutagenesis; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020033:Protein Isoforms / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D017384:Sequence Deletion; D012694:Serine / Q000235:genetics; D014364:Tryptophan / Q000235:genetics
C577836:ABCA1 protein, human; D064286:ATP Binding Cassette Transporter 1; D018528:ATP-Binding Cassette Transporters; D016632:Apolipoprotein A-I; D008076:Cholesterol, HDL; D010446:Peptide Fragments; D020033:Protein Isoforms; D012694:Serine; D014364:Tryptophan